Mass Spectrometry Analysis Of Cross-Linked Amino Acids In Cardiac Collagen
Keywords
Heart Failure, Collagen, Cross-Linked Amino Acids, Mass Spectrometry, Precursor Ion Scanning
Abstract
Heart failure may be related to abnormal cross-linking of cardiac collagen, because the cross-linking process determines the mechanical strength of cardiac collagen. Studies have shown that the content of certain cross-linked amino acids can be used as molecular markers corresponding to abnormal collagen cross-linking, but the molecular markers for abnormal cardiac collagen cross-linking are still unclear. This study established a tandem mass spectrometry analysis method that can detect two important cross-linked amino acids in hydrolyzed collagen proteins – pyridinoline (PYD) and deoxypyridinoline (DPD) with high selectivity. DPD was detected in the acidic hydrolyzate of mouse ventricular collagen, but PYD was not detected, indicating that PYD has nothing to do with the cross-linking process of cardiac collagen, while DPD plays a more important role in the cross-linking of cardiac collagen and may become a factor related to the cross-linking of cardiac collagen. Molecular markers associated with heart failure. This study provides a mass spectrometry-based method for studying cardiac collagen cross-linked products, which can also be used for the analysis of other collagens.
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Original research was done by Jiang Wei , Yu Gang
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